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Literature summary extracted from

  • Chandel, M.; Azmi, W.
    Purification and characterization of tyrosine phenol lyase from Citrobacter freundii (2013), Appl. Biochem. Biotechnol., 171, 2040-2052.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.99.2 synthesis tyrosine phenol lyase is an important enzyme for the synthesis of pharmaceutical aromatic amino acids, viz. L-tyrosine and L-DOPA Citrobacter freundii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.99.2 0.446
-
L-tyrosine pH 8.5, 30°C Citrobacter freundii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.99.2 intracellular
-
Citrobacter freundii 5622
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.2 52000
-
4 * 52000, SDS-PAGE Citrobacter freundii
4.1.99.2 220000
-
native enzyme, native PAGE Citrobacter freundii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.2 L-3-4 dihydroxyphenylalanine + H2O Citrobacter freundii L-DOPA, alpha-beta elimination catechol + pyruvate + NH3
-
r
4.1.99.2 L-tyrosine + H2O Citrobacter freundii alpha-beta elimination phenol + pyruvate + NH3
-
r

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.2 Citrobacter freundii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.2 native enzyme 35fold to homogeneity by ammonium sulfate fractionation, dialysis, and hydrophobic interaction chromatography Citrobacter freundii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.99.2 1.1
-
purified enzyme, pH 8.5, 30°C Citrobacter freundii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.2 L-3-4 dihydroxyphenylalanine + H2O L-DOPA, alpha-beta elimination Citrobacter freundii catechol + pyruvate + NH3
-
r
4.1.99.2 L-asparagine + H2O
-
Citrobacter freundii ?
-
?
4.1.99.2 L-methionine + H2O
-
Citrobacter freundii ?
-
?
4.1.99.2 L-phenylalanine + H2O low activity Citrobacter freundii ?
-
?
4.1.99.2 L-tyrosine + H2O alpha-beta elimination Citrobacter freundii phenol + pyruvate + NH3
-
r
4.1.99.2 L-valine + H2O
-
Citrobacter freundii ?
-
?
4.1.99.2 additional information alanine, arginine, aspartate, cysteine, glutamine, glutamate, glycine, histidine, isoleucine, leucine, lysine, proline, serine, threonine, tryptophan are poor or no substrates, substrate specificity of purified tyrosine phenol lyase, overview Citrobacter freundii ?
-
?

Subunits

EC Number Subunits Comment Organism
4.1.99.2 More N-terminal sequences comparisons, overview Citrobacter freundii
4.1.99.2 tetramer 4 * 52000, SDS-PAGE Citrobacter freundii

Synonyms

EC Number Synonyms Comment Organism
4.1.99.2 tyrosine phenol lyase
-
Citrobacter freundii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.2 45
-
-
Citrobacter freundii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.1.99.2 30 55 activity range, profile, overview Citrobacter freundii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.99.2 35
-
purified native enzyme, half-life is 130 min Citrobacter freundii
4.1.99.2 45
-
purified native enzyme, half-life is 52 min Citrobacter freundii
4.1.99.2 55
-
purified native enzyme, half-life is 10 min Citrobacter freundii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.2 8.5
-
-
Citrobacter freundii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.2 pyridoxal 5'-phosphate dependent on, highest activity at 0.015-0.02 mM Citrobacter freundii

General Information

EC Number General Information Comment Organism
4.1.99.2 metabolism tyrosine phenol lyase catalyses the biosynthesis of L-tyrosine/L-DOPA from ammonium, pyruvate and phenolic substrates through the reverse of alpha- and beta-elimination reaction Citrobacter freundii